The signaling mucins Msb2 and Hkr1 differentially regulate the filamentation mitogen-activated protein kinase pathway and contribute to a multimodal response.
about
The Caenorhabditis elegans mucin-like protein OSM-8 negatively regulates osmosensitive physiology via the transmembrane protein PTR-23The filamentous growth MAPK Pathway Responds to Glucose Starvation Through the Mig1/2 transcriptional repressors in Saccharomyces cerevisiaeScaffold Protein Ahk1, Which Associates with Hkr1, Sho1, Ste11, and Pbs2, Inhibits Cross Talk Signaling from the Hkr1 Osmosensor to the Kss1 Mitogen-Activated Protein KinaseProper protein glycosylation promotes mitogen-activated protein kinase signal fidelityShedding of the mucin-like flocculin Flo11p reveals a new aspect of fungal adhesion regulation.Multiple plant surface signals are sensed by different mechanisms in the rice blast fungus for appressorium formationSimilar environments but diverse fates: Responses of budding yeast to nutrient deprivationYeast osmosensors Hkr1 and Msb2 activate the Hog1 MAPK cascade by different mechanisms.Multiple signals converge on a differentiation MAPK pathway.The yeast sphingolipid signaling landscape.Global regulation of a differentiation MAPK pathway in yeast.Epitope-guided engineering of monobody binders for in vivo inhibition of Erk-2 signaling.Cdc42p-interacting protein Bem4p regulates the filamentous-growth mitogen-activated protein kinase pathway.Role of the unfolded protein response in regulating the mucin-dependent filamentous-growth mitogen-activated protein kinase pathway.Post-translational regulation of signaling mucins.Metabolic respiration induces AMPK- and Ire1p-dependent activation of the p38-Type HOG MAPK pathway.Vacuolar H+-ATPase works in parallel with the HOG pathway to adapt Saccharomyces cerevisiae cells to osmotic stressComparative Analysis of Transmembrane Regulators of the Filamentous Growth Mitogen-Activated Protein Kinase Pathway Uncovers Functional and Regulatory DifferencesTEAK: topology enrichment analysis framework for detecting activated biological subpathways.Genetic networks inducing invasive growth in Saccharomyces cerevisiae identified through systematic genome-wide overexpressionSpatial landmarks regulate a Cdc42-dependent MAPK pathway to control differentiation and the response to positional compromise.Dissecting Gene Expression Changes Accompanying a Ploidy-Based Phenotypic Switch.Stress signalling to fungal stress-activated protein kinase pathways.Choosing the right lifestyle: adhesion and development in Saccharomyces cerevisiae.The regulation of filamentous growth in yeast.Response to hyperosmotic stressFunctional genomics in the study of yeast cell polarity: moving in the right direction.Single-cell analysis reveals that insulation maintains signaling specificity between two yeast MAPK pathways with common components.Role of phosphatidylinositol phosphate signaling in the regulation of the filamentous-growth mitogen-activated protein kinase pathway.Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1.Binding of the Extracellular Eight-Cysteine Motif of Opy2 to the Putative Osmosensor Msb2 Is Essential for Activation of the Yeast High-Osmolarity Glycerol Pathway.The tRNA modification complex elongator regulates the Cdc42-dependent mitogen-activated protein kinase pathway that controls filamentous growth in yeast.The impact of protein glycosylation on Flo11-dependent adherence in Saccharomyces cerevisiae.Unfolding dynamics of the mucin SEA domain probed by force spectroscopy suggest that it acts as a cell-protective device.Sho1 and Msb2-related proteins regulate appressorium development in the smut fungus Ustilago maydis.Msb2 signaling mucin controls activation of Cek1 mitogen-activated protein kinase in Candida albicans.Role of the cell wall integrity and filamentous growth mitogen-activated protein kinase pathways in cell wall remodeling during filamentous growth.Stress Adaptation.The membrane mucin Msb2 regulates invasive growth and plant infection in Fusarium oxysporum.Activation of the signalling mucin MoMsb2 and its functional relationship with Cbp1 in Magnaporthe oryzae.
P2860
Q27343144-F73D6A21-2CA3-4230-8C00-E10C095DC5B8Q27932392-61FB560F-97D7-454A-802A-0936AC270D07Q27934789-311E7B36-9DC9-496E-9B6D-0ABE4B2D6C9DQ27937276-F00EB649-5D65-4ECA-8BC9-3B327E9604D3Q27939435-02AEAC7C-3F72-496B-99AB-7D54D03B2BE7Q28476784-44D22ACE-8E30-42A3-8757-C2EA1004D642Q28590330-266A376E-DED4-4877-932A-3577AD364F56Q30009456-9751E630-8C15-42AF-B018-759234D3E4BEQ33545219-93741543-2010-404D-8FE4-FC0E2918E368Q34414198-4728E518-65F7-442E-8406-46C50816D9A5Q34471632-31798115-CCD7-42E6-835B-917438774FC6Q34507603-16BA1E51-BD9E-4B49-A654-6A99B7F81CB9Q34745471-6E54ABD4-4BEE-4016-865B-0C774281D0BFQ35214693-3B920FA7-FA42-42B1-A8A8-6FA9AA20B6FFQ35291869-4F31885F-195A-4A17-9C90-A1ABE700B6FBQ35376992-B6E26D68-B7EB-4FCF-9D0F-5FBB3FA013D9Q35804688-697FDF91-57C2-479C-8541-9F040D257EC5Q36001598-5DF6E440-D696-4714-9776-353B362643F2Q36580942-72714EBD-CCB6-4F4F-9509-57D424A2DD2EQ36709972-5DB83554-D6D1-463F-A1B3-D54D9ADCA06CQ36802383-353E4B15-3181-472E-9076-122D3532A12EQ37565743-B507510C-405D-40AF-994A-D0C13ED1F988Q37719594-2B57463C-F567-48CB-B3B7-CF499F9BEB7EQ37869191-D57C2DDA-EED5-4D82-84A2-E3385F97BF3CQ37973321-4712A15E-7DFD-41C1-ACB5-2FCF791CE8B5Q38048770-38C10041-C4AF-41D8-BB7A-CAED039E2C8CQ38142052-9712165F-0FD1-4C2C-B81F-FB7F5A7F8604Q38884642-A049B67C-D855-42FE-BCFF-26F05CD3573FQ39247190-C2D2E7C6-8157-4CEF-B966-520088B3AD3FQ39991319-309799DB-87CB-4F98-8F6E-E16BC90B8B48Q40284251-F36E1095-A541-45A5-BEA7-B7F494540616Q41888858-A662D41D-F86A-4999-BF13-4255381D4608Q42112332-6BFCF826-6D17-4812-9C9B-93A334C077EFQ42558893-D87A1665-1075-4E3E-BF37-05B3BBC533B3Q43001712-16885548-A5F3-49FB-A246-6F1BCF097F52Q43071889-82C2BC64-9745-48AE-BA69-FAAD8E0C2590Q43071903-A7B0816C-2012-46F8-8E11-5F0681953B39Q46334030-6EFDF3A2-E940-413C-8198-B1FD9627B2B7Q46441464-7B294DD2-C532-4E6D-968D-D4ACF9F79E6DQ52956290-0E908D33-B22E-47AA-8865-CC88E7DFFDF8
P2860
The signaling mucins Msb2 and Hkr1 differentially regulate the filamentation mitogen-activated protein kinase pathway and contribute to a multimodal response.
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
The signaling mucins Msb2 and ...... bute to a multimodal response.
@ast
The signaling mucins Msb2 and ...... bute to a multimodal response.
@en
The signaling mucins Msb2 and ...... bute to a multimodal response.
@nl
type
label
The signaling mucins Msb2 and ...... bute to a multimodal response.
@ast
The signaling mucins Msb2 and ...... bute to a multimodal response.
@en
The signaling mucins Msb2 and ...... bute to a multimodal response.
@nl
prefLabel
The signaling mucins Msb2 and ...... bute to a multimodal response.
@ast
The signaling mucins Msb2 and ...... bute to a multimodal response.
@en
The signaling mucins Msb2 and ...... bute to a multimodal response.
@nl
P2093
P2860
P356
P1476
The signaling mucins Msb2 and ...... ibute to a multimodal response
@en
P2093
Andrew Pitoniak
Barbara Birkaya
Nadia Vadaie
Paul J Cullen
P2860
P304
P356
10.1091/MBC.E08-07-0760
P407
P577
2009-05-13T00:00:00Z